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HEADER HYDROLASE 14-SEP-04 1WPX
TITLE CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE Y INHIBITOR COMPLEXED
TITLE 2 WITH THE COGNATE PROTEINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYPEPTIDASE Y;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBOXYPEPTIDASE YSCY;
COMPND 5 EC: 3.4.16.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CARBOXYPEPTIDASE Y INHIBITOR;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: CPY INHIBITOR, IC, IC, DKA1 PROTEIN, NSP1 PROTEIN,
COMPND 10 TFS1 PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 6 ORGANISM_COMMON: YEAST
KEYWDS CARBOXYPEPTIDASE INHIBITOR, SERINE PROTEINASE INHIBITOR,
KEYWDS 2 PROTEINASE-INHIBITOR COMPLEX, PHOSPHATIDYLETHANOLAMINE-
KEYWDS 3 BINDING PROTEIN, PHOSPHOLIPID
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MIMA,M.HAYASHIDA,T.FUJII,Y.NARITA,R.HAYASHI,M.UEDA,Y.HATA
REVDAT 1 01-MAR-05 1WPX 0
JRNL AUTH J.MIMA,M.HAYASHIDA,T.FUJII,Y.NARITA,R.HAYASHI,
JRNL AUTH 2 M.UEDA,Y.HATA
JRNL TITL STRUCTURE OF THE CARBOXYPEPTIDASE Y INHIBITOR I(C)
JRNL TITL 2 IN COMPLEX WITH THE COGNATE PROTEINASE REVEALS A
JRNL TITL 3 NOVEL MODE OF THE PROTEINASE-PROTEIN INHIBITOR
JRNL TITL 4 INTERACTION
JRNL REF J.MOL.BIOL. V. 346 1323 2005
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1566324.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 27780
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2456
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4386
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 179
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4960
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.93000
REMARK 3 B22 (A**2) : -7.25000
REMARK 3 B33 (A**2) : -0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.82
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 40.48
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CAPPING.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : CAPPING.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WPX COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-2004.
REMARK 100 THE RCSB ID CODE IS RCSB023865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JAN-2004
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 4.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 1.95M AMMONIUM
REMARK 280 SULFATE, PH 4.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.56450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.57000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 93.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.57000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.56450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 93.29500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS B 573
REMARK 465 SER B 574
REMARK 465 VAL B 575
REMARK 465 PRO B 576
REMARK 465 GLN B 577
REMARK 465 ALA B 578
REMARK 465 GLU B 622
REMARK 465 ALA B 623
REMARK 465 THR B 624
REMARK 465 HIS B 625
REMARK 465 GLU B 626
REMARK 465 THR B 627
REMARK 465 SER B 628
REMARK 465 GLY B 629
REMARK 465 ALA B 630
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 241 CG ASN A 241 OD1 0.092
REMARK 500 ASN A 241 CG ASN A 241 ND2 -0.101
REMARK 500 ASN A 305 CG ASN A 305 OD1 0.099
REMARK 500 ASN A 305 CG ASN A 305 ND2 -0.096
REMARK 500 ASN B 502 CG ASN B 502 OD1 0.101
REMARK 500 ASN B 502 CG ASN B 502 ND2 -0.098
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 14 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 THR A 18 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU A 21 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 VAL A 23 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 GLU A 65 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU A 66 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 SER A 70 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 THR A 89 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 PRO A 96 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU A 178 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 TYR A 187 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 GLY A 194 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASN A 299 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 VAL A 377 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 VAL B 546 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 GLY B 549 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 VAL B 664 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG B 685 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 10 -72.57 38.94
REMARK 500 SER A 146 -119.55 60.66
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BD9 RELATED DB: PDB
REMARK 900 RELATED ID: 1BEH RELATED DB: PDB
REMARK 900 RELATED ID: 1A44 RELATED DB: PDB
REMARK 900 RELATED ID: 1QOU RELATED DB: PDB
REMARK 900 RELATED ID: 1FJJ RELATED DB: PDB
REMARK 900 RELATED ID: 1FUX RELATED DB: PDB
DBREF 1WPX A 1 421 SWS P00729 CBPY_YEAST 112 532
DBREF 1WPX B 501 719 SWS P14306 CPYI_YEAST 1 219
SEQADV 1WPX ACE B 500 SWS P14306 ACETYLATION
SEQRES 1 A 421 LYS ILE LYS ASP PRO LYS ILE LEU GLY ILE ASP PRO ASN
SEQRES 2 A 421 VAL THR GLN TYR THR GLY TYR LEU ASP VAL GLU ASP GLU
SEQRES 3 A 421 ASP LYS HIS PHE PHE PHE TRP THR PHE GLU SER ARG ASN
SEQRES 4 A 421 ASP PRO ALA LYS ASP PRO VAL ILE LEU TRP LEU ASN GLY
SEQRES 5 A 421 GLY PRO GLY CYS SER SER LEU THR GLY LEU PHE PHE GLU
SEQRES 6 A 421 LEU GLY PRO SER SER ILE GLY PRO ASP LEU LYS PRO ILE
SEQRES 7 A 421 GLY ASN PRO TYR SER TRP ASN SER ASN ALA THR VAL ILE
SEQRES 8 A 421 PHE LEU ASP GLN PRO VAL ASN VAL GLY PHE SER TYR SER
SEQRES 9 A 421 GLY SER SER GLY VAL SER ASN THR VAL ALA ALA GLY LYS
SEQRES 10 A 421 ASP VAL TYR ASN PHE LEU GLU LEU PHE PHE ASP GLN PHE
SEQRES 11 A 421 PRO GLU TYR VAL ASN LYS GLY GLN ASP PHE HIS ILE ALA
SEQRES 12 A 421 GLY GLU SER TYR ALA GLY HIS TYR ILE PRO VAL PHE ALA
SEQRES 13 A 421 SER GLU ILE LEU SER HIS LYS ASP ARG ASN PHE ASN LEU
SEQRES 14 A 421 THR SER VAL LEU ILE GLY ASN GLY LEU THR ASP PRO LEU
SEQRES 15 A 421 THR GLN TYR ASN TYR TYR GLU PRO MET ALA CYS GLY GLU
SEQRES 16 A 421 GLY GLY GLU PRO SER VAL LEU PRO SER GLU GLU CYS SER
SEQRES 17 A 421 ALA MET GLU ASP SER LEU GLU ARG CYS LEU GLY LEU ILE
SEQRES 18 A 421 GLU SER CYS TYR ASP SER GLN SER VAL TRP SER CYS VAL
SEQRES 19 A 421 PRO ALA THR ILE TYR CYS ASN ASN ALA GLN LEU ALA PRO
SEQRES 20 A 421 TYR GLN ARG THR GLY ARG ASN VAL TYR ASP ILE ARG LYS
SEQRES 21 A 421 ASP CYS GLU GLY GLY ASN LEU CYS TYR PRO THR LEU GLN
SEQRES 22 A 421 ASP ILE ASP ASP TYR LEU ASN GLN ASP TYR VAL LYS GLU
SEQRES 23 A 421 ALA VAL GLY ALA GLU VAL ASP HIS TYR GLU SER CYS ASN
SEQRES 24 A 421 PHE ASP ILE ASN ARG ASN PHE LEU PHE ALA GLY ASP TRP
SEQRES 25 A 421 MET LYS PRO TYR HIS THR ALA VAL THR ASP LEU LEU ASN
SEQRES 26 A 421 GLN ASP LEU PRO ILE LEU VAL TYR ALA GLY ASP LYS ASP
SEQRES 27 A 421 PHE ILE CYS ASN TRP LEU GLY ASN LYS ALA TRP THR ASP
SEQRES 28 A 421 VAL LEU PRO TRP LYS TYR ASP GLU GLU PHE ALA SER GLN
SEQRES 29 A 421 LYS VAL ARG ASN TRP THR ALA SER ILE THR ASP GLU VAL
SEQRES 30 A 421 ALA GLY GLU VAL LYS SER TYR LYS HIS PHE THR TYR LEU
SEQRES 31 A 421 ARG VAL PHE ASN GLY GLY HIS MET VAL PRO PHE ASP VAL
SEQRES 32 A 421 PRO GLU ASN ALA LEU SER MET VAL ASN GLU TRP ILE HIS
SEQRES 33 A 421 GLY GLY PHE SER LEU
SEQRES 1 B 220 ACE MET ASN GLN ALA ILE ASP PHE ALA GLN ALA SER ILE
SEQRES 2 B 220 ASP SER TYR LYS LYS HIS GLY ILE LEU GLU ASP VAL ILE
SEQRES 3 B 220 HIS ASP THR SER PHE GLN PRO SER GLY ILE LEU ALA VAL
SEQRES 4 B 220 GLU TYR SER SER SER ALA PRO VAL ALA MET GLY ASN THR
SEQRES 5 B 220 LEU PRO THR GLU LYS ALA ARG SER LYS PRO GLN PHE GLN
SEQRES 6 B 220 PHE THR PHE ASN LYS GLN MET GLN LYS SER VAL PRO GLN
SEQRES 7 B 220 ALA ASN ALA TYR VAL PRO GLN ASP ASP ASP LEU PHE THR
SEQRES 8 B 220 LEU VAL MET THR ASP PRO ASP ALA PRO SER LYS THR ASP
SEQRES 9 B 220 HIS LYS TRP SER GLU PHE CYS HIS LEU VAL GLU CYS ASP
SEQRES 10 B 220 LEU LYS LEU LEU ASN GLU ALA THR HIS GLU THR SER GLY
SEQRES 11 B 220 ALA THR GLU PHE PHE ALA SER GLU PHE ASN THR LYS GLY
SEQRES 12 B 220 SER ASN THR LEU ILE GLU TYR MET GLY PRO ALA PRO PRO
SEQRES 13 B 220 LYS GLY SER GLY PRO HIS ARG TYR VAL PHE LEU LEU TYR
SEQRES 14 B 220 LYS GLN PRO LYS GLY VAL ASP SER SER LYS PHE SER LYS
SEQRES 15 B 220 ILE LYS ASP ARG PRO ASN TRP GLY TYR GLY THR PRO ALA
SEQRES 16 B 220 THR GLY VAL GLY LYS TRP ALA LYS GLU ASN ASN LEU GLN
SEQRES 17 B 220 LEU VAL ALA SER ASN PHE PHE TYR ALA GLU THR LYS
MODRES 1WPX ASN A 87 ASN GLYCOSYLATION SITE
MODRES 1WPX ASN A 168 ASN GLYCOSYLATION SITE
MODRES 1WPX ASN A 368 ASN GLYCOSYLATION SITE
HET ACE B 500 3
HET NAG A 810 14
HET NAG A 820 14
HET NAG A 830 14
HET SO4 901 5
HET SO4 902 5
HETNAM ACE ACETYL GROUP
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETSYN NAG NAG
FORMUL 2 ACE C2 H3 O1
FORMUL 3 NAG 3(C8 H15 N1 O6)
FORMUL 6 SO4 2(O4 S1 2-)
FORMUL 8 HOH *51(H2 O1)
HELIX 1 1 ASP A 4 LEU A 8 5 5
HELIX 2 2 SER A 58 PHE A 64 1 7
HELIX 3 3 SER A 83 ASN A 87 5 5
HELIX 4 4 ASN A 111 PHE A 130 1 20
HELIX 5 5 PRO A 131 LYS A 136 1 6
HELIX 6 6 TYR A 147 HIS A 162 1 16
HELIX 7 7 ASP A 180 TYR A 185 1 6
HELIX 8 8 TYR A 187 CYS A 193 1 7
HELIX 9 9 PRO A 203 GLN A 228 1 26
HELIX 10 10 SER A 229 LEU A 245 1 17
HELIX 11 11 LEU A 245 THR A 251 1 7
HELIX 12 12 THR A 271 ASN A 280 1 10
HELIX 13 13 GLN A 281 GLY A 289 1 9
HELIX 14 14 ASN A 299 PHE A 308 1 10
HELIX 15 15 HIS A 317 GLN A 326 1 10
HELIX 16 16 ASN A 342 LEU A 353 1 12
HELIX 17 17 TYR A 357 GLN A 364 1 8
HELIX 18 18 MET A 398 VAL A 403 1 6
HELIX 19 19 VAL A 403 HIS A 416 1 14
HELIX 20 20 MET B 501 ILE B 505 5 5
HELIX 21 21 ASP B 506 HIS B 518 1 13
HELIX 22 22 GLY B 519 VAL B 524 1 6
HELIX 23 23 PRO B 553 ARG B 558 5 6
HELIX 24 24 ASP B 675 PHE B 679 5 5
HELIX 25 25 ARG B 685 TYR B 690 5 6
HELIX 26 26 GLY B 696 GLU B 703 1 8
SHEET 1 A11 ILE A 2 LYS A 3 0
SHEET 2 A11 GLN A 16 ASP A 22 -1 O THR A 18 N LYS A 3
SHEET 3 A11 HIS A 29 PHE A 35 -1 O THR A 34 N TYR A 17
SHEET 4 A11 THR A 89 LEU A 93 -1 O PHE A 92 N TRP A 33
SHEET 5 A11 VAL A 46 LEU A 50 1 N TRP A 49 O ILE A 91
SHEET 6 A11 PHE A 140 GLU A 145 1 O ALA A 143 N LEU A 48
SHEET 7 A11 SER A 171 GLY A 175 1 O LEU A 173 N ILE A 142
SHEET 8 A11 ILE A 330 GLY A 335 1 O LEU A 331 N ILE A 174
SHEET 9 A11 PHE A 387 VAL A 392 1 O THR A 388 N VAL A 332
SHEET 10 A11 VAL A 377 TYR A 384 -1 N LYS A 382 O TYR A 389
SHEET 11 A11 ARG A 367 THR A 370 -1 N TRP A 369 O GLY A 379
SHEET 1 B 2 SER A 69 ILE A 71 0
SHEET 2 B 2 PRO A 77 GLY A 79 -1 O ILE A 78 N SER A 70
SHEET 1 C 6 ALA B 544 VAL B 546 0
SHEET 2 C 6 GLY B 534 SER B 541 -1 N SER B 541 O ALA B 544
SHEET 3 C 6 GLN B 562 ASN B 568 -1 O GLN B 562 N GLU B 539
SHEET 4 C 6 PHE B 633 ASN B 639 -1 O SER B 636 N PHE B 565
SHEET 5 C 6 PHE B 609 LEU B 619 -1 N LYS B 618 O ASN B 639
SHEET 6 C 6 ASN B 644 ILE B 647 -1 O ASN B 644 N CYS B 615
SHEET 1 D 8 ALA B 544 VAL B 546 0
SHEET 2 D 8 GLY B 534 SER B 541 -1 N SER B 541 O ALA B 544
SHEET 3 D 8 GLN B 562 ASN B 568 -1 O GLN B 562 N GLU B 539
SHEET 4 D 8 PHE B 633 ASN B 639 -1 O SER B 636 N PHE B 565
SHEET 5 D 8 PHE B 609 LEU B 619 -1 N LYS B 618 O ASN B 639
SHEET 6 D 8 PHE B 589 ASP B 595 -1 N PHE B 589 O LEU B 617
SHEET 7 D 8 HIS B 661 LYS B 669 -1 O TYR B 668 N THR B 590
SHEET 8 D 8 GLN B 707 ALA B 716 -1 O VAL B 709 N LEU B 667
SSBOND 1 CYS A 56 CYS A 298
SSBOND 2 CYS A 193 CYS A 207
SSBOND 3 CYS A 217 CYS A 240
SSBOND 4 CYS A 224 CYS A 233
SSBOND 5 CYS A 262 CYS A 268
LINK ND2 ASN A 87 C1 NAG A 810
LINK ND2 ASN A 168 C1 NAG A 820
LINK ND2 ASN A 368 C1 NAG A 830
CISPEP 1 GLY A 53 PRO A 54 0 -0.10
CISPEP 2 GLN A 95 PRO A 96 0 -0.23
CISPEP 3 ALA B 598 PRO B 599 0 -0.08
CRYST1 81.129 186.590 65.140 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012326 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005359 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015352 0.00000
TER 3344 LEU A 421
TER 4962 LYS B 719
MASTER 316 0 6 26 27 0 0 6 5063 2 68 50
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